Sequences in both class ii major histocompatibility complex α and β chains contribute to the binding of the superantigen toxic shock syndrome toxin 1

Ned S. Braunstein, Dominique A. Weber, Xiao Cun Wang, Eric O. Long, David Karp

Research output: Contribution to journalArticlepeer-review

28 Scopus citations

Abstract

Class II major histocompatibility complex (MFIC) molecules present peptides derived from processed antigen to antigen-specific CD4-positive T cells. In addition, class II molecules bind with high affinity another class of antigens, termed superantigens. T cell stimulation by superantigens depends almost exclusively on the Vβ segment expressed by the T ceil receptor (TCR). Mapping of the superantigen binding site on class II molecules should provide valuable information on how MHC and TCR molecules interact. Recombinant mouse I-A class II molecules expressed on transfected L cells were analyzed for their ability to bind the toxic shock syndrome toxin 1. Polymorphic residues in the α helices of both the α and β chains of I-A contributed to quantitative toxin binding, suggesting that the toxin binds to either a combinatorial or a conformational site on class II MHC molecules.

Original languageEnglish (US)
Pages (from-to)1301-1305
Number of pages5
JournalJournal of Experimental Medicine
Volume175
Issue number5
DOIs
StatePublished - May 1 1992

ASJC Scopus subject areas

  • Immunology and Allergy
  • Immunology

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